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- PDB-2l04: The Solution Structure of the C-terminal Ig-like Domain of the Ba... -

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Basic information

Entry
Database: PDB / ID: 2l04
TitleThe Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube Protein
ComponentsMajor tail protein V
KeywordsVIRAL PROTEIN / bacteriophage lambda / phage tail / gpV / Ig-like domain
Function / homology
Function and homology information


virus tail, tube / symbiont genome ejection through host cell envelope, long flexible tail mechanism / viral tail assembly / host cell cytoplasm
Similarity search - Function
Immunoglobulin-like - #1080 / Lambda phage tail tube protein / Lambda phage tail tube protein, TTP / Bacterial Ig-like domain (group 2) / Bacterial Ig-like domain 2 / Bacterial Ig-like domain, group 2 / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesEnterobacteria phage lambda (virus)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsPell, L.G. / Gasmi-Seabrook, G.M.C. / Donaldson, L.W. / Howell, P. / Davidson, A.R. / Maxwell, K.L.
CitationJournal: J.Mol.Biol. / Year: 2010
Title: The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage l Tail Tube Protein.
Authors: Pell, L.G. / Gasmi-Seabrook, G.M. / Morais, M. / Neudecker, P. / Kanelis, V. / Bona, D. / Donaldson, L.W. / Edwards, A.M. / Howell, P.L. / Davidson, A.R. / Maxwell, K.L.
History
DepositionJun 30, 2010Deposition site: BMRB / Processing site: RCSB
Revision 1.0Sep 22, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Jun 19, 2013Group: Database references
Revision 1.3Feb 5, 2020Group: Database references / Other / Category: pdbx_database_status / struct_ref_seq_dif
Item: _pdbx_database_status.status_code_cs / _struct_ref_seq_dif.details
Revision 1.4May 1, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Major tail protein V


Theoretical massNumber of molelcules
Total (without water)8,8821
Polymers8,8821
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Major tail protein V


Mass: 8882.022 Da / Num. of mol.: 1 / Fragment: C-terminal, UNP residues 160-246
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Enterobacteria phage lambda (virus) / Gene: V / Plasmid: pET32b / Production host: Escherichia coli (E. coli) / References: UniProt: P03733

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D CBCA(CO)NH
1313D HN(CA)CB
1423D (H)CCH-TOCSY
1513D HNCO
1613D C(CO)NH
1713D 1H-15N NOESY
1823D 1H-13C NOESY
1913D H(CCO)NH

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Sample preparation

Details
Solution-IDContentsSolvent system
150 mM sodium phosphate-1, 200 mM sodium chloride-2, 90% H2O/10% D2O90% H2O/10% D2O
250 mM sodium phosphate-3, 200 mM sodium chloride-4, 100% D2O100% D2O
Sample
Conc. (mg/ml)ComponentSolution-ID
50 mMsodium phosphate-11
200 mMsodium chloride-21
50 mMsodium phosphate-32
200 mMsodium chloride-42
Sample conditionsIonic strength: 0.2 / pH: 6.8 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz

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Processing

NMR software
NameDeveloperClassification
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
CYANAGuntert, Mumenthaler and Wuthrichrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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